IBPA_SALTY
ID IBPA_SALTY Reviewed; 137 AA.
AC Q7CPF1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Small heat shock protein IbpA {ECO:0000255|HAMAP-Rule:MF_02000};
DE AltName: Full=16 kDa heat shock protein A {ECO:0000255|HAMAP-Rule:MF_02000};
GN Name=ibpA {ECO:0000255|HAMAP-Rule:MF_02000}; OrderedLocusNames=STM3809;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Associates with aggregated proteins, together with IbpB, to
CC stabilize and protect them from irreversible denaturation and extensive
CC proteolysis during heat shock and oxidative stress. Aggregated proteins
CC bound to the IbpAB complex are more efficiently refolded and
CC reactivated by the ATP-dependent chaperone systems ClpB and
CC DnaK/DnaJ/GrpE. Its activity is ATP-independent. {ECO:0000255|HAMAP-
CC Rule:MF_02000}.
CC -!- SUBUNIT: Monomer. Forms homomultimers of about 100-150 subunits at
CC optimal growth temperatures. Conformation changes to monomers at high
CC temperatures or high ionic concentrations. {ECO:0000255|HAMAP-
CC Rule:MF_02000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02000}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|HAMAP-Rule:MF_02000, ECO:0000255|PROSITE-
CC ProRule:PRU00285}.
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DR EMBL; AE006468; AAL22668.1; -; Genomic_DNA.
DR RefSeq; NP_462709.3; NC_003197.2.
DR RefSeq; WP_001532742.1; NC_003197.2.
DR AlphaFoldDB; Q7CPF1; -.
DR SMR; Q7CPF1; -.
DR STRING; 99287.STM3809; -.
DR PaxDb; Q7CPF1; -.
DR EnsemblBacteria; AAL22668; AAL22668; STM3809.
DR GeneID; 1255336; -.
DR KEGG; stm:STM3809; -.
DR PATRIC; fig|99287.12.peg.4032; -.
DR HOGENOM; CLU_046737_4_2_6; -.
DR PhylomeDB; Q7CPF1; -.
DR BioCyc; SENT99287:STM3809-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050821; P:protein stabilization; IEA:UniProtKB-UniRule.
DR CDD; cd06470; ACD_IbpA-B_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR HAMAP; MF_02000; HSP20_IbpA; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR037913; ACD_IbpA/B.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR023728; HSP20_IbpA.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..137
FT /note="Small heat shock protein IbpA"
FT /id="PRO_0000126024"
FT DOMAIN 28..137
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ SEQUENCE 137 AA; 15750 MW; 13EF8A31032A3453 CRC64;
MRNFDLSPLY RSAIGFDRLF NLLENNQSQS NGGYPPYNVE LVDENHYRIA IAVAGFAESE
LEITAQDNLL VVKGAHADEQ KERTYLYQGI AERNFERKFQ LAENIHVRGA NLVNGLLYIE
LERVIPEANK PRRIEIN
